Microtubule-based perception of mechanical conflicts controls plant organ morphogenesis.

Precise coordination between cells and tissues is essential for differential growth in plants. During lateral root formation in , the endodermis is actively remodeled to allow outgrowth of the new organ. Here, we show that microtubule arrays facing lateral root founder cells display a higher order compared to arrays on the opposite side of the same cell, and this asymmetry is required for endodermal remodeling and lateral root initiation.

VAPYRIN-like is required for development of the moss .

The () gene in and is required for arbuscular mycorrhizal (AM) symbiosis. The moss has a close homolog (, ), although it does not form AM. Here, we explore the phylogeny of and in land plants, and study the expression and developmental function of in We show that is expressed primarily in the protonema, the early filamentous stage of moss development, and later in rhizoids arising from the leafy gametophores and in adult phyllids.

RMR (Receptor Membrane RING-H2) type 1 and 2 show different promoter activities and subcellular localizations in Arabidopsis thaliana.

Soluble vacuolar proteins reach their compartments of final accumulation through the binding with specific transmembrane cargo receptors. In Arabidopsis thaliana two different families of receptors have been characterized. The AtVSRs (Vacuolar Sorting Receptor), which are known to be involved in the protein sorting to lytic vacuoles (LV), and the AtRMRs (Receptor Membrane RING-H2), for which there is less evidence for a role in the traffic to the protein storage vacuole (PSV).

The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain.

The tonoplast was proposed as a default destination of membrane-bound proteins without specific targeting signals. To investigate the nature of this targeting, we created type I fusion proteins with green fluorescent protein followed by the transmembrane domain of the human lysosomal protein LAMP1. We varied the length of the transmembrane domain from 23 to either 20 or 17 amino acids by deletion within the hydrophobic domain.

Regeneration of a lytic central vacuole and of neutral peripheral vacuoles can be visualized by green fluorescent proteins targeted to either type of vacuoles.

Protein trafficking to two different types of vacuoles was investigated in tobacco (Nicotiana tabacum cv SR1) mesophyll protoplasts using two different vacuolar green fluorescent proteins (GFPs). One GFP is targeted to a pH-neutral vacuole by the C-terminal vacuolar sorting determinant of tobacco chitinase A, whereas the other GFP is targeted to an acidic lytic vacuole by the N-terminal propeptide of barley aleurain, which contains a sequence-specific vacuolar sorting determinant. The trafficking and final accumulation in the central vacuole (CV) or in smaller peripheral vacuoles differed for the two reporter proteins, depending on the cell type.

Specific accumulation of GFP in a non-acidic vacuolar compartment via a C-terminal propeptide-mediated sorting pathway.

The green fluorescent protein (GFP) from Aequorea victoria can be detected in living plant cells after transient transformation of protoplasts. Expression of the GFP can be used to monitor protein trafficking in a mixed cell population and also to study the different function and importance of organelles in different cell types. We developed a vacuolar form of GFP that was obtained by replacing the C-terminal endoplasmic reticulum (ER)-retention motif of mGFP5-ER by the vacuolar targeting peptide of tobacco chitinase A.

Analysis of the 22 kbp long psbD-psbC gene cluster of Euglena gracilis chloroplast DNA: evidence for overlapping transcription units undergoing differential processing.

The clustered genes psbD and psbC covering together close to 22,000 nucleotides contain ten and eleven exons, respectively. The corresponding translation products, i.e, Photosystem II core 34 kDa (D2) protein and the CP43 chlorophyll binding protein are highly conserved.

Cloning and sequencing of a corn (Zea mays) nuclear gene coding for the chloroplast specific catalytic subunit of ferredoxin-thioredoxin reductase.

We determined the complete nucleotide sequence of a cDNA clone encoding the smaller, catalytic subunit of ferredoxin-thioredoxin reductase from corn chloroplasts. The translated protein sequence, representing a subunit of 12.9 kDa shows 80% identity with the protein sequence from spinach and contains seven Cys residues all at conserved positions.

Analysis of streptomycin-resistance of Escherichia coli mutants.

We previously reported about Escherichia coli transformation experiments yielding streptomycin-resistant cells carrying a C912 to T transition in a plasmid-born 16S rRNA gene. These experiments were based on results obtained with streptomycin-resistant Euglena chloroplasts bearing an equivalent mutation in the single chloroplast 16S rRNA gene. We extended this study and transformed E.

Polypeptide composition of rotavirus empty capsids and their possible use as a subunit vaccine.

Two types of empty capsid particles that differed with respect to the presence of the two outer shell proteins were isolated from MA-104 cells infected with bovine rotavirus V1005. Three previously uncharacterized polypeptides, I, II, and III, migrating between VP2 and VP6, were detected in empty capsids but not in single- and double-shelled rotavirus particles. Peptide mapping revealed that all three proteins were related to VP2.

Characterization of a second bovine rotavirus serotype.

Bovine rotavirus (BRV) V 1005 was characterized by two-way cross-neutralization tests as a second serotype of BRV. Virions and inner shell particles of 65 nm and 55 nm diameter respectively, and empty capsids of 65 nm and 55 nm diameter were separated by density gradient centrifugation. Three polypeptides of molecular weight 60,000, 36,000 and 28,000 (minor protein) could be identified in the outer shell of virions and in the larger empty capsids.